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Article

Unscrambling thermal stability and temperature adaptation in evolved variants of a cold-active lipase.

FEBS letters - 25 Jun 2008

Gatti-Lafranconi Pietro, Caldarazzo Serena M, Villa Alessandra, Alberghina Lilia, Lotti Marina

Abstract excerpt

Directed evolution by error-prone PCR was applied to stabilize the cold-active lipase from Pseudomonas fragi (PFL). PFL displays high activity at 10 degrees C, but it is highly unstable even at moderate temperatures. After two rounds of evolution, a variant was generated with a 5-fold increase in half-life at 42 degrees C and a shift of 10 degrees C in the temperature optimum, nevertheless retaining...

Read the complete abstract on PubMed

Topics

Amino Acid Sequence
Bacterial Proteins
Cold Temperature
Directed Molecular Evolution
Enzyme Stability
Hot Temperature

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Lipase

Molecular Sequence Data

Mutation

Protein Conformation

Pseudomonas fragi

Source

Identifiers

PMID: 18534193
DOI: 10.1016/j.febslet.2008.05.037

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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